P60_LISIN
ID P60_LISIN Reviewed; 467 AA.
AC Q01836;
DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT 16-NOV-2001, sequence version 2.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=Probable endopeptidase p60;
DE EC=3.4.-.-;
DE AltName: Full=Invasion-associated protein p60;
DE Flags: Precursor;
GN Name=iap; OrderedLocusNames=lin0591;
OS Listeria innocua serovar 6a (strain ATCC BAA-680 / CLIP 11262).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Listeriaceae; Listeria.
OX NCBI_TaxID=272626;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Serovar 6b;
RX PubMed=1514809; DOI=10.1128/aem.58.8.2625-2632.1992;
RA Bubert A., Koehler S., Goebel W.;
RT "The homologous and heterologous regions within the iap gene allow
RT genus- and species-specific identification of Listeria spp. by polymerase
RT chain reaction.";
RL Appl. Environ. Microbiol. 58:2625-2632(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-680 / CLIP 11262;
RX PubMed=11679669; DOI=10.1126/science.1063447;
RA Glaser P., Frangeul L., Buchrieser C., Rusniok C., Amend A., Baquero F.,
RA Berche P., Bloecker H., Brandt P., Chakraborty T., Charbit A.,
RA Chetouani F., Couve E., de Daruvar A., Dehoux P., Domann E.,
RA Dominguez-Bernal G., Duchaud E., Durant L., Dussurget O., Entian K.-D.,
RA Fsihi H., Garcia-del Portillo F., Garrido P., Gautier L., Goebel W.,
RA Gomez-Lopez N., Hain T., Hauf J., Jackson D., Jones L.-M., Kaerst U.,
RA Kreft J., Kuhn M., Kunst F., Kurapkat G., Madueno E., Maitournam A.,
RA Mata Vicente J., Ng E., Nedjari H., Nordsiek G., Novella S., de Pablos B.,
RA Perez-Diaz J.-C., Purcell R., Remmel B., Rose M., Schlueter T., Simoes N.,
RA Tierrez A., Vazquez-Boland J.-A., Voss H., Wehland J., Cossart P.;
RT "Comparative genomics of Listeria species.";
RL Science 294:849-852(2001).
RN [3]
RP DISCUSSION OF SEQUENCE.
RX PubMed=1459966; DOI=10.1128/jb.174.24.8166-8171.1992;
RA Bubert A., Kuhn M., Goebel W., Koehler S.;
RT "Structural and functional properties of the p60 proteins from different
RT Listeria species.";
RL J. Bacteriol. 174:8166-8171(1992).
CC -!- FUNCTION: This major extracellular protein may be involved in the
CC invasion of non-professional phagocytic cells by Listeria.
CC -!- DOMAIN: LysM domains are thought to be involved in peptidoglycan
CC binding.
CC -!- SIMILARITY: Belongs to the peptidase C40 family. {ECO:0000255|PROSITE-
CC ProRule:PRU01284, ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAC95823.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; M80349; AAA25283.1; -; Genomic_DNA.
DR EMBL; AL596165; CAC95823.1; ALT_INIT; Genomic_DNA.
DR PIR; AG1506; AG1506.
DR AlphaFoldDB; Q01836; -.
DR STRING; 272626.lin0591; -.
DR CAZy; CBM50; Carbohydrate-Binding Module Family 50.
DR EnsemblBacteria; CAC95823; CAC95823; CAC95823.
DR KEGG; lin:iap; -.
DR eggNOG; COG0791; Bacteria.
DR eggNOG; COG1388; Bacteria.
DR eggNOG; COG3103; Bacteria.
DR HOGENOM; CLU_581142_0_0_9; -.
DR Proteomes; UP000002513; Chromosome.
DR GO; GO:0008234; F:cysteine-type peptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd00118; LysM; 2.
DR Gene3D; 3.10.350.10; -; 2.
DR InterPro; IPR018392; LysM_dom.
DR InterPro; IPR036779; LysM_dom_sf.
DR InterPro; IPR000064; NLP_P60_dom.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR003646; SH3-like_bac-type.
DR Pfam; PF01476; LysM; 2.
DR Pfam; PF00877; NLPC_P60; 1.
DR Pfam; PF08239; SH3_3; 1.
DR SMART; SM00257; LysM; 2.
DR SMART; SM00287; SH3b; 1.
DR SUPFAM; SSF54001; SSF54001; 1.
DR SUPFAM; SSF54106; SSF54106; 2.
DR PROSITE; PS51782; LYSM; 2.
DR PROSITE; PS51935; NLPC_P60; 1.
DR PROSITE; PS51781; SH3B; 1.
PE 3: Inferred from homology;
KW Hydrolase; Protease; Repeat; Signal; Thiol protease.
FT SIGNAL 1..27
FT /evidence="ECO:0000250"
FT CHAIN 28..467
FT /note="Probable endopeptidase p60"
FT /id="PRO_0000019758"
FT DOMAIN 28..71
FT /note="LysM 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01118"
FT DOMAIN 79..143
FT /note="SH3b"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01117"
FT DOMAIN 199..242
FT /note="LysM 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01118"
FT DOMAIN 349..467
FT /note="NlpC/P60"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01284"
FT REGION 154..199
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 247..348
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 330..343
FT /note="7 X 2 AA tandem repeats of T-N"
FT COMPBIAS 162..183
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 268..348
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 379
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01284"
FT ACT_SITE 429
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01284"
FT ACT_SITE 441
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01284"
FT VARIANT 240
FT /note="L -> P (in strain: Serovar 6B)"
FT VARIANT 328
FT /note="K -> KNTNTNTNTNTNTNT (in strain: Serovar 6B)"
SQ SEQUENCE 467 AA; 49044 MW; 0F40B031BD2175C1 CRC64;
MNMKKATIAA TAGIAVTAFA APTIASASTV VVEAGDTLWG IAQSKGTTVD AIKKANNLTT
DKIVPGQKLQ VNEVATEEKA EKSVSATWLN VRSGAGVDHS ILTSIKGGTK VTVETTESNG
WHKITYNDGK TGYVNGKYLT DKATSTPVVK QEVKKETTQQ VKPATEAKTE VKQPTTQQTA
PAPKAAETKE APVVDQNATT HNVKSGDTIW ALSVKYGVSV QDIMSWNNLS SSSIYVGQKL
AIKQPTKTVA PKAETKTQAP AAEKQTAPAV KENSNANTAT TEKKETATEQ QTTTKAPTQA
AKPAPAPSTN TNKTNTTNNN TNASTPSKNT NTNTNTNTNT NTNQGSTNNA SASALIAEAQ
KHLGKAYSWG GNGPTTFDCS GFTKYVFAKS GISLPRTSGA QYASTTRISE SQAKPGDLVF
FDYGSGISHV GIYVGNGQMI NAQDNGVKYD NIHGAGWGKF LVGFGRV